Purchase

Description

Background Information

Transferrin is related to several other iron-binding proteins including lactoferrin, melanotransferrin, and ovotransferin. These molecules comprise the transferrin superfamily. All members of this superfamily have similar polypeptide folding patterns. The N-terminal and C-terminal domains of these proteins are globular moieties of about 330 amino acids. Each of these domains is divided into two subdomains, with the iron- and anion-binding sites found within the intersubdomain cleft. The binding cleft opens with iron release, and closes with iron binding.

Applications

All cells require iron for the proper uptake of oxygen from their environment. Transferrin, a protein isolated from serum, causes the uptake and transport of iron from culture medium to the cells. This allows proper oxygen uptake and also stimulates growth-related enzyme activity. Iron-saturated transferrin (holo transferrin) is continually recycled after releasing iron and becomes iron-deficient transferrin (apo-transferrin). Choosing which form to use depends upon the culture conditions. In media such as Dulbecco′s Modified Eagle′s Medium/Ham′s Nutrient Mixture F12 (DMEM/F12) that contain high levels of iron salt, using apo-transferrin is preferred.

Product Description

Transferrin is a glycoprotein with homologous N-terminal and C-terminal iron-binding domains.